Preparation and process optimization of xanthine oxidase inhibitory peptides from Trachinotus ovatus

  • HOU Mengfan ,
  • HU Xiao ,
  • YANG Xianqing ,
  • CHEN Shengjun ,
  • WU Yanyan ,
  • XU Jiachao
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  • 1(College of Food Science and Engineering,Ocean University of China,Qingdao 266003,China)
    2(Key Laboratory of Aquatic Product Processing,Ministry of Agriculture and Rural Affairs,South China Sea Fisheries Research Institute,Chinese Academy of Fishery Science,Guangzhou 510300,China)

Received date: 2021-03-15

  Revised date: 2021-04-10

  Online published: 2021-12-31

Abstract

In this study, Trachinotus ovatus muscle was hydrolyzed with different proteases to obtain xanthine oxidase (XOD) inhibitory peptides. The degree of hydrolysis and the XOD inhibition activity were used as evaluation index, and the optimum hydrolysis conditions were obtained by single factor analysis and response surface methodology. Then, the molecular weight distribution and amino acids composition of the hydrolysates were investigated. The results showed that neutral protease was the optimal enzyme, and the optimum hydrolysis conditions were as follows: the solid-liquid ratio of 1∶3 (g∶mL), the hydrolysis temperature of 54 ℃ and pH 7.0 for 5 h, with the enzyme dosage of 0.19%. Under these conditions, the hydrolysis degree and XOD inhibitory activity were 11.82% and 52.41% respectively, which was consistent with the predicted values. The molecular weight of the peptides obtained by this method was mainly less than 3 000 Da (account for 93.92%). Its hydrophobic amino acid content was as high as 36.95%, and rich in Leu, Ala, Val and Ile. The results provide reference for the intensive processing and high-value utilization of T.ovatus.

Cite this article

HOU Mengfan , HU Xiao , YANG Xianqing , CHEN Shengjun , WU Yanyan , XU Jiachao . Preparation and process optimization of xanthine oxidase inhibitory peptides from Trachinotus ovatus[J]. Food and Fermentation Industries, 2021 , 47(23) : 185 -192 . DOI: 10.13995/j.cnki.11-1802/ts.027276

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